Structure of PDB 5fbz Chain C

Receptor sequence
>5fbzC (length=433) Species: 79882 (Sutcliffiella halmapala) [Search protein sequence]
NDVARGIVKADVAQNNFGLYGQGQIVAVADTGLDTGRNDSSMHEAFRGKI
TALYALGRTNNANDPNGHGTHVAGSVLGNATNKGMAPQANLVFQSIMDSG
GGLGGLPANLQTLFSQAYSAGARIHTNSWGAPVNGAYTTDSRNVDDYVRK
NDMTILFAAGNEGPGSGTISAPGTAKNAITVGATENLRPSFGSYADNINH
VAQFSSRGPTRDGRIKPDVMAPGTYILSARSSLAPDSSFWANHDSKYAYM
GGTSMATPIVAGNVAQLREHFVKNRGVTPKPSLLKAALIAGAADVGLGFP
NGNQGWGRVTLDKSLNVAFVNETSPLSTSQKATYSFTAQAGKPLKISLVW
SDAPGSTTASLTLVNDLDLVITAPNGTKYVGNDFTAPYDNNWDGRNNVEN
VFINAPQSGTYTVEVQAYNVPVGPQTFSLAIVH
3D structure
PDB5fbz Stabilization of Enzymes by Metal Binding: Structures of Two Alkalophilic Bacillus Subtilases and Analysis of the Second Metal-Binding Site of the Subtilase Family
ChainC
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D30 H68 N161 S254
Catalytic site (residue number reindexed from 1) D30 H68 N161 S254
Enzyme Commision number 3.4.21.14: Transferred entry: 3.4.21.62, 3.4.21.63, 3.4.21.64, 3.4.21.65 and 3.4.21.67.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA C E185 S193 D196 H200 E185 S193 D196 H200
BS02 CA C D366 L367 D368 D393 E399 D366 L367 D368 D393 E399
BS03 CA C D383 T385 P387 N390 N391 D383 T385 P387 N390 N391
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:5fbz, PDBe:5fbz, PDBj:5fbz
PDBsum5fbz
PubMed
UniProtA0A182DWC7

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